Molecular cloning, overexpression and biochemical characterization of hypothetical β-lactamases of Mycobacterium tuberculosis H37Rv

Journal of Applied Microbiology

Volumn 105, Issue 1, 2008, Pages 59-67

  Nampoothiri, K M ^a   Rubex, R ^a   Patel, A K ^a   Narayanan, S S ^a   Krishna, S ^a   Das, S M ^a   Pandey, A ^a  

^a REGIONAL RESEARCH LABORATORY CSIR   (India)

Author keywords

Mycobacterium tuberculosis; Nitrocefin; lactam antibiotics; lactamases

Indexed keywords

AMIDES; ANTIBIOTICS; CLONING; ENZYME INHIBITION; ESCHERICHIA COLI; GENE ENCODING; TUBES (COMPONENTS);

BIOCHEMICAL CHARACTERIZATION; M. TUBERCULOSIS; METHOD ANALYSIS; MOLECULAR CLONING; MYCOBACTERIUM TUBERCULOSIS; NITROCEFIN; OVEREXPRESSIONS; RESULT ANALYSIS; Β-LACTAM ANTIBIOTICS; Β-LACTAMASE;

RECOMBINANT PROTEINS;

AMOXICILLIN; AMOXICILLIN PLUS CLAVULANIC ACID; AMPICILLIN; BACTERIAL ENZYME; BETA LACTAM; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CARBENICILLIN; CEFALORIDINE; CEFAZOLIN; CEFOTAXIME; GENE PRODUCT; KANAMYCIN; NITROCEFIN; PENICILLIN G; POLYHISTIDINE TAG; RECOMBINANT PROTEIN;

ANTIBIOTIC RESISTANCE; BACTERIUM; BIOCHEMISTRY; CATALYSIS; ENZYME ACTIVITY; GENE EXPRESSION; GENOME; HYDROLYSIS; INHIBITION; MOLECULAR ANALYSIS; PROTEIN; RECOMBINATION; TUBERCULOSIS;

ANTIBIOTIC RESISTANCE; ANTIBIOTIC SENSITIVITY; ARTICLE; BACTERIAL GENE; BACTERIAL GENOME; BACTERIAL STRAIN; BIOCHEMISTRY; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; ESCHERICHIA COLI; EXPRESSION VECTOR; GENE OVEREXPRESSION; HYDROLYSIS; IMMUNOBLOTTING; MOLECULAR CLONING; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PREDICTION;

ESCHERICHIA COLI; MYCOBACTERIUM TUBERCULOSIS;

EID: 44849124472     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/j.1365-2672.2007.03721.x     Document Type: Article

References (36)

1. Abate, G. Miorner, H. (1998) Susceptibility of multi drug resistant strains of Mycobacterium tuberculosis to amoxycillin (sic) in combination with clavulanic acid and ethambutol. J Antimicrob Chemother 42, 735 740.
2. Amsterdam, D. (1996) Susceptibility testing of antimicrobials in liquid media. In Antibiotics in Laboratory Medicine, Fourth Edition ed. Lorian, V. pp. 52 111 Baltimore, MD : Williams & Wilkins.
3. Bradford, M.M. (1976) A rapid and sensitive for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248 254.
4. Bush, K., Jacoby, G.A. Medeiro, A.A. (2005) A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob Agents Chemother 39, 1211 1233.
5. Casal, M.J., Rodriguez, F.C., Luna, M.D. Benavente, M.C. (1987) In vitro susceptibility of Mycobacterium tuberculosis, Mycobacterium africanum, Mycobacterium bovis, Mycobacterium avium, Mycobacterium fortuitum, and Mycobacterium chelonae to ticarcillin in combination with clavulanic acid. Antimicrob Agents Chemother 31, 132 133.
6. Chaba, R., Raje, M. Chakraborti, P.K. (2002) Evidence that a eukaryotic-type serine/threonine protein kinase from Mycobacterium tuberculosis regulates morphological changes associated with cell division. Eur J Biochem 269, 1078 1085.
7. Chambers, H.F., Moreau, D., Yaj, D., Miick, C., Wagner, C., Hackbarth, C., Kocagoz, S., Rosenberg, E. et al. (1995) Can penicillin and other beta lactam antibiotics be used to treat tuberculosis? Antimicrob Agents Chemother 39, 2620 2624.
8. Edwards, R., Beringer, R. Greenwood, D. (1996) Characterization of β-lactamases of Prevotella species. Anaerobe 2, 217 221.
9. Felmingham, D. Gruneberg, R.N. (1996) A multi collaborative study of the antimicrobial susceptibility of community - acquired lower respiratory tract pathogens 1992-1993: The Alexander project. J Antimicrob Chemother 38, 1 57.
10. Flores, A.R., Parsons, L.M. Pavelkara, M.S. Jr. (2005a) Characterization of novel Mycobacterium tuberculosis and Mycobacterium smegmatis mutants hyper susceptible to β-lactam antibiotics. J Bacteriol 187, 1892 1900.
11. Flores, A.R., Parsons, L.M. Pavelkara, M.S. Jr. (2005b) Genetic analysis of the β- lactamases of Mycobacterium tuberculosis and Mycobacterium smegmatis and susceptibility to β-lactam antibiotics. Microbiology 15, 1521 532.
12. Gasteiger, E., Gattiker, A., Hoogland, C., Ivanyi, I., Appel, R.D. Bairoch, A. (2003) ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res 31, 3784 3788.
13. Hackbarth, C.J., Unsal, I. Chambers, H.F. (1997) Cloning and sequence analysis of a class A β-lactamase from Mycobacterium tuberculosis H37Ra. Antimicrob Agents Chemother 41, 1182 1185.
14. Kaneda, S. Yabu, K. (1983) Purification and some properties of β-lactamase from M. smegmatis. Microbiol Immunol 27, 191 193.
15. Kasik, J.E. (1979) Mycobacterial beta-lactamases. In β-Lactamases ed. Hamilton-Miller, J.M.T. Smith, J.T. pp. 339 350 London, UK : Academic Press.
16. Kwon, H.H., Tomioka, H. Saito, H. (1995) Distribution and characterization of b-lactamases of mycobacteria and related organisms. Tuber Lung Dis 76, 141 148.
17. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature 227, 680 685.
18. Li, X.Z, Zhang, L. Nikaido, H. (2004) Efflux pump mediated intrinsic drug resistance in M. smegmatis. Antimicrob Agents Chemother 48, 2415 2423.
19. Marchler-Bauer, A. Bryant, S.S.H. (2004) CD-Search: protein domain annotations on the fly. Nucleic Acids Res 32, 327 331.
20. Massova, I. Mobashery, S. (1998) Kinship and diversification of bacterial penicillin-binding proteins and β-lactamases. Antimicrob Agents Chemother 42, 1 17.
21. Matagne, A., Joris, B. Frere, J.M. (1991) J.M. Anomalous behaviour of a protein during SDS/PAGE corrected by chemical modification of carboxylic groups. Biochem J 280, 553 556.
22. McDonough, J.A., Hacker, E., Flores, A.R., Pavelka, M.S. Jr. Braunstein, M. (2005) The twin-arginine translocation pathway of Mycobacterium smegmatis is functional for the export of Mycobacterial β-lactamases. J Bacteriol 187, 7667 7679.
23. Motley, S.T. Lory, S. (1999) Functional characterization of a serine/ threonine protein kinase of Pseudomonas aeruginosa. Infect Immun 67, 5386 5394.
24. Nadler, J.P., Berger, J., Nord, J.A., Cofsky, R. Saxena, M. (1991) Amoxicillin/clavulanic acid for treating drug resistant Mycobacterium tuberculosis. Chest 99, 1025 1026.
25. Nampoothiri, K.M. (2003) Mycobacterial β-lactamases: an Overview. Ind J Biotechnol 2, 342 345.
26. O'Callaghan, C.H., Morris, A., Kirby, S.M. Shingler, A.H. (1972) Novel method for detection of β-lactamases by using a chromogenic cephalosporin substrate. Antimicrob Agents Chemother 1, 283 288.
27. Prabhakaran, K., Harris, E.B. Randhawa, B. (1999) Bactericidal action of ampicillin/sulbactam against intracellular mycobacteria. Int J Antimicrob Agent 13, 133 135.
28. 2155 β-lactamase. FEMS Microbiol Lett 149, 11 15.
29. Sambrook, J., Fritsch, F.E. Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd edn. Cold Spring Harbor, NY : Cold Spring Harbor Laboratory.
30. Segura, C., Salvado, M., Collado, I., Chaves, J. Coira, A. (1998) Contribution of β-lactamases to β-lactam susceptibilities of susceptible and multidrug-resistant M. tuberculosis clinical isolates. Antimicrob Agents Chemother 42, 1524 1526.
31. Takenouchi, T., Ishii, Y. Yamaguchi, K. (2002) Properties of extended-spectrum β-lactamases constructed by site-directed mutagenesis. J Infect Chemother 8, 211 217.
32. Therrien, C. Levesque, R.C. (2000) Molecular basis of antibiotic resistance and β-lactamase inhibition by mechanism based inactivators: perspectives and future directions. FEMS Microbiol Rev 24, 251 262.
33. Utrup, L.J., Moore, T.D., Actor, P. Poupard, J.A. (1995) Susceptibilities of non tuberculosis mycobacterial species to amoxicillinclavulanic acid alone and in combination with antimycobacterial agents. Antimicrob Agents Chemother 39, 1454 1457.
34. Voladri, R.K., Lakey, D.L., Hennigan, S.H., Menzies, B.E., Edwards, K.M. Kernodle, D.S. (1998) Recombinant expression and characterization of the major β-lactamases of Mycobacterium tuberculosis. Antimicrob Agents Chemother 42, 1375 1381.
35. Wang, F., Cassidi, C. Sacchettini, J.C. (2006) Crystal structure and activity studies of the Mycobacterium tuberculosisβ-lactamase reveal its critical role in resistance to β- lactam antibiotics. Antimicrob Agents Chemother 50, 2762 2771.
36. Yabu, K., Kaneda, S. Ochiai, T. (1985) Relationship between b-lactamase activity and resistance to β-lactam antibiotics in Mycobacterium smegmatis. Microbiol Immunol 29, 803 809.